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X-ray diffraction
2.3Å resolution

Leishmania TDR1 - a unique trimeric glutathione transferase

Released:
DOI: 10.2210/pdb4ags/pdb
PDB 4ags coloured by chain and viewed from the front.
PDB 4ags coloured by chain and viewed from the side.
PDB 4ags coloured by chain and viewed from the top.
Source organism: Leishmania infantum
Primary publication:
Leishmania TDR1 structure, a unique trimeric glutathione transferase capable of deglutathionylation and antimonial prodrug activation.
Fyfe PK, Westrop GD, Silva AM, Coombs GH, Hunter WN
Proc. Natl. Acad. Sci. U.S.A. (2012)
PMID: 22753509

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thiol-dependent reductase 1 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 471 amino acids
Theoretical weight: 53.2 KDa
Source organism: Leishmania infantum
Expression system: Escherichia coli B
UniProt:
  • Canonical: A4I8P2 (Residues: 1-450; Coverage: 100%)
Gene names: LINJ_33_0260, TDR1
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand GSH 6 x GSH
Ligand EDO 15 x EDO
1 modified residue:
Ligand MSE 51 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: C2
Unit cell:
a: 197.477Å b: 58.396Å c: 160.385Å
α: 90° β: 111.81° γ: 90°
R-values:
R R work R free
0.152 0.149 0.208
Expression system: Escherichia coli B

Quick links

Citations

7 review citations

Polyamine-Based Thiols in Trypanosomatids: Evolution, Protein Structural Adaptations, and Biological Functions.
Manta et al. (2018)
6 more

3 mentions without citation

Leishmania TDR1 structure, a unique trimeric glutathione transferase capable of deglutathionylation and antimonial prodrug activation.
Fyfe et al. (2012)
2 more